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- *********************************************
- * Ubiquitin-conjugating enzymes active site *
- *********************************************
-
- Ubiquitin-conjugating enzymes (EC 6.3.2.19) (UBC or E2 enzymes) [1,2,3]
- catalyze the covalent attachment of ubiquitin to target proteins. An activated
- ubiquitin moiety is transferred from an ubiquitin-activating enzyme (E1) to E2
- which later ligates ubiquitin directly to substrate proteins with or without
- the assistance of 'N-end' recognizing proteins (E3).
-
- In most species there are many forms of UBC (at least 9 in yeast) which are
- implicated in diverse cellular functions.
-
- A cysteine residue is required for ubiquitin-thiolester formation. There is a
- single conserved cysteine in UBC's and the region around that residue is
- conserved in the sequence of known UBC isozymes. We have used that region as
- a signature pattern.
-
- -Consensus pattern: [FYWL]-H-[PC]-N-[LIV]-x(3,4)-G-x-[LIV]-C-[LIV]-x-[LIV]
- [C is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for yeast UBC6 (DOA2).
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: June 1994 / Text revised.
-
- [ 1] Jentsch S., Seufert W., Sommer T., Reins H.-A.
- Trends Biochem. Sci. 15:195-198(1990).
- [ 2] Jentsch S., Seufert W., Hauser H.-P.
- Biochim. Biophys. Acta 1089:127-139(1991).
- [ 3] Hershko A.
- Trends Biochem. Sci. 16:265-268(1991).
-